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Related Concept Videos

Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

6.6K
Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
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Ion Channels01:19

Ion Channels

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The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
Ion channels are specialized integral membrane proteins on the plasma membrane that allow...
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ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

8.4K
ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
8.4K
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

4.8K
GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
4.8K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

5.5K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
5.5K
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

12.6K
Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...
12.6K

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Updated: Aug 23, 2025

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

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Biomimetic Artificial Proton Channels.

Iuliana-Marilena Andrei1, Mihail Barboiu1

  • 1Adaptative Supramolecular Nanosystems Group, Institut Europeen des Membranes, University of Montpellier, ENSCM-CNRS, Place E. Bataillon CC047, 34095 Montpellier, France.

Biomolecules
|October 27, 2022
PubMed
Summary
This summary is machine-generated.

Artificial proton channels mimic biological systems for efficient proton transfer across membranes. This review covers their design, self-assembly, and transport activity, offering insights for future applications.

Keywords:
H-bondingbilayer-membranesion-channelsproton transportself-assembly

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Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
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Area of Science:

  • Biochemistry and Biophysics
  • Materials Science
  • Nanotechnology

Background:

  • Proton transfer across cell membranes is a fundamental biochemical process vital for physiological functions.
  • While extensively studied, the precise mechanistic details of proton translocation remain incompletely understood.
  • Artificial proton channels are emerging as a key area of research to elucidate these mechanisms.

Purpose of the Study:

  • To provide a comprehensive overview of the development of artificial proton channels.
  • To analyze the design principles, self-assembly, and proton transport capabilities of these synthetic channels.
  • To compare the performance of artificial channels with natural protein proton channels.

Main Methods:

  • Review of existing literature on artificial proton channel design and synthesis.
  • Analysis of experimental data on proton transport activity in artificial channels embedded in bilayer membranes.
  • Comparative studies contrasting artificial and protein-based proton channel functionalities.

Main Results:

  • Detailed examination of various artificial proton channel architectures and their self-assembly properties.
  • Evaluation of proton transport efficiency and mechanisms in different artificial channel systems.
  • Identification of key factors, including confined water and channel components, influencing proton dynamics.

Conclusions:

  • Artificial proton channels offer promising platforms for understanding fundamental proton transfer processes.
  • Their design and self-assembly are crucial for efficient proton transport activity.
  • Further research holds potential for significant applications in various scientific and technological fields.